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PDBsum entry 1gpp
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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High resolution crystal structure of domain i of the saccharomyces cerevisiae homing endonuclease pi-Scei.
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Authors
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E.Werner,
W.Wende,
A.Pingoud,
U.Heinemann.
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Ref.
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Nucleic Acids Res, 2002,
30,
3962-3971.
[DOI no: ]
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PubMed id
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Abstract
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The homing endonuclease PI-SceI from Saccharo myces cerevisiae consists of two
domains. The protein splicing domain I catalyzes the excision of the mature
endonuclease (intein) from a precursor protein and the religation of the
flanking amino acid sequences (exteins) to a functional protein. Furthermore,
domain I is involved in binding and recognition of the specific DNA substrate.
Domain II of PI-SceI, the endonuclease domain, which is structurally homologous
to other homing endonucleases from the LAGLIDADG family, harbors the
endonucleolytic center of PI-SceI, which in vivo initiates the homing process by
introducing a double-strand cut in the approximately 35 bp recognition sequence.
At 1.35 A resolution, the crystal structure of PI-SceI domain I provides a
detailed view of the part of the protein that is responsible for tight and
specific DNA binding. A geometry-based docking of the 75 degrees bent
recognition sequence to the full-length protein implies a conformational change
or hinge movement of a subdomain of domain I, the tongs part, that is predicted
to reach into the major groove near base pairs +16 to +18.
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